The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Identity verification passed. The target is unambiguously human KIF1A—kinesin family member 1A, UniProt Q12756, aliases ATSV, C2orf20, hUnc-104—not a similarly named gene. The literature consistently describes the mammalian/human protein as a neuron-enriched kinesin-3, microtubule-based mechanochemical ATPase. Its N-terminal kinesin motor, neck/coiled-coil regions, FHA domain and C-terminal PH-containing cargo-binding region agree with the supplied InterPro/UniProt annotation. Caenorhabditis elegans UNC-104 is the ortholog and is used below only as comparative or model-system evidence, never as the human protein itself. (chiba2023insightintothe pages 1-2, chai2024aplantflavonol pages 1-2)
KIF1A’s primary function is ATP-driven, predominantly plus-end-directed transport of neuronal membrane cargo—especially synaptic-vesicle precursors (SVPs), dense-core vesicles and active-zone precursor material—from the neuronal soma through axons toward presynaptic terminals. ATP is its enzymatic substrate; vesicles are its transported cargo rather than biochemical substrates. Its physiological importance lies in supplying distant synapses with membrane proteins and release machinery, thereby supporting synapse formation, neurotransmission, neuronal survival and circuit plasticity. (chiba2023insightintothe pages 1-2, vitet2023huntingtinrecruitskif1a pages 1-2)
| Feature | Current annotation | Evidence basis | Key caveat |
|---|---|---|---|
| Identity and organism | KIF1A, kinesin family member 1A; human UniProt Q12756; aliases include ATSV, C2orf20 and hUnc-104. | Human KIF1A disease studies, purified-human-protein assays and mammalian neuronal studies consistently describe the same kinesin-3 axonal motor; no conflicting gene-symbol usage was identified. (anazawa2022denovomutations pages 10-11, chiba2023insightintothe pages 1-2, benoit2024cryoemunveilskinesin pages 1-2) | UNC-104 is the C. elegans ortholog, not the human protein; worm findings are evolutionary or functional inference unless independently reproduced with human or mammalian KIF1A. |
| Protein class and enzymatic reaction | N-terminal kinesin-3 mechanochemical ATPase in the TRAFAC myosin–kinesin ATPase class; hydrolyzes ATP and couples chemical energy to microtubule movement: ATP + H₂O → ADP + phosphate. | Reviews identify KIF1A as an ATP-powered microtubule motor; human structures show nucleotide-state-dependent motor-head and neck-linker conformations. (chiba2023insightintothe pages 1-2, benoit2024cryoemunveilskinesin pages 1-2) | ATP is the biochemical substrate; membrane vesicles are transported cargo, not enzymatic substrates. Exact kinetics depend on construct and assay conditions. |
| Domain architecture | N-terminal kinesin motor domain followed by a neck-coil and coiled-coil-rich stalk, an FHA domain and a C-terminal pleckstrin-homology domain. | Human-protein and conserved UNC-104/KIF1A literature supports this architecture; the PH domain binds PIP₂-containing artificial vesicles. (chiba2023insightintothe pages 1-2, chai2024aplantflavonol pages 1-2) | Some domain-function assignments derive partly from orthologs and engineered constructs. No residue coordinates are asserted. |
| Direction and track | Moves processively toward microtubule plus ends. Predominantly plus-end-out axonal microtubules therefore support anterograde transport from the soma toward presynaptic terminals. | Supported by established kinesin directionality, neuronal microtubule polarity, mammalian cargo-transport experiments and human KIF1A–microtubule structures. (chiba2023insightintothe pages 1-2, vitet2023huntingtinrecruitskif1a pages 1-2, benoit2024cryoemunveilskinesin pages 1-2) | Dendritic microtubules have mixed polarity, so motor directionality alone does not determine axonal versus dendritic cargo entry. |
| Motor activation and processivity | Autoinhibited KIF1A is modeled as compact and predominantly monomeric in solution; activation promotes dimerization and coordinated two-headed stepping. Its positively charged K-loop contacts α- and β-tubulin tails and supports rapid rebinding and superprocessivity. | A 2023 review integrates biochemical and structural evidence; 2024 cryo-EM resolved one- and two-head-bound human KIF1A states at 2.7–3.5 Å and reported runs exceeding 1,000 steps under suitable in-vitro conditions. (chiba2023insightintothe pages 1-2, benoit2024cryoemunveilskinesin pages 1-2) | Oligomeric state and autoinhibition are context-dependent. Purified systems do not fully reproduce crowded axons, cargo membranes or microtubule-associated proteins. |
| Principal cargos | Best-supported cargos are synaptic-vesicle precursors and synaptic-vesicle-associated carriers. KIF1A also transports dense-core vesicles and active-zone precursor material; lysosomal transport occurs in selected contexts. | Mammalian neurons, mouse genetics and reviews support these cargo classes; KIF1A-deficient mice accumulate SVPs in cell bodies and lose synaptic vesicles at terminals. (chiba2023insightintothe pages 1-2, vitet2023huntingtinrecruitskif1a pages 1-2, hummel2021specifickif1a–adaptorinteractions pages 1-2) | Synaptic vesicles and their precursors are not always experimentally separable. Cargo composition varies among species, neuronal types and maturation states. |
| Cargo recognition and regulators | Cargo selection and activation involve lipid binding and regulators including Rab3–DENN/MADD, vesicle-associated Arl8, huntingtin and liprin-α/TANC2. Liprin-α/TANC2 may act mainly as synaptic signposts rather than classical vesicle adaptors. | Rab3–MADD and Arl8 mechanisms draw on mammalian and conserved UNC-104 studies. A 2023 mouse study found that phosphorylated huntingtin recruits KIF1A to SVPs; KIF1A silencing normalized excessive transport and motor-learning defects. (chiba2023insightintothe pages 8-8, vitet2023huntingtinrecruitskif1a pages 1-2, hummel2021specifickif1a–adaptorinteractions pages 1-2) | Evidence that Arl8 releases autoinhibition is especially strong for C. elegans UNC-104. Physical association does not necessarily establish a direct motor–cargo bridge. |
| Cellular localization | A cytosolic motor recruited dynamically to microtubules and cargo membranes; enriched in neurons and active from soma through axonal shafts to presynaptic terminals. Dense-core-vesicle transport also occurs in dendrites. | Live-neuron transport, mouse loss-of-function and cargo-relocalization experiments support axonal and dendritic activity. (vitet2023huntingtinrecruitskif1a pages 1-2, chiba2023insightintothe pages 1-2, hummel2021specifickif1a–adaptorinteractions pages 1-2) | KIF1A is not a fixed organelle-resident protein. Overexpressed fluorescent constructs may differ from endogenous localization. |
| Physiological role | Supplies distal neuronal compartments with presynaptic membrane proteins, neuropeptide-containing vesicles and active-zone components, supporting synapse formation, neurotransmitter release, neuronal survival and circuit plasticity. | Mouse KIF1A loss causes somatic SVP accumulation, fewer terminal synaptic vesicles, sensorimotor deficits and early death. Increased huntingtin-dependent recruitment elevated SVP transport and release probability but impaired motor learning. (vitet2023huntingtinrecruitskif1a pages 1-2) | Both deficient and excessive transport can be harmful; normal function requires regulated cargo flux rather than maximal motor activity. |
| Disease mechanism | Pathogenic variants cause KIF1A-associated neurological disorder, encompassing neurodevelopmental, spastic-paraplegia and sensory-neuropathy phenotypes. Variants can reduce microtubule binding, force or motility, relieve autoinhibition and cause hypermotility, or dominantly impair wild-type/mutant heterodimers. | Human-variant biochemistry, single-molecule assays and CRISPR worm models support loss-of-function, gain-of-function and dominant-negative mechanisms. More than 100 point variants had been reported by the 2023 review. (anazawa2022denovomutations pages 10-11, chiba2023insightintothe pages 1-2, benoit2024cryoemunveilskinesin pages 1-2) | Mechanism is allele-specific; KAND is not uniformly caused by haploinsufficiency. Worm findings require confirmation in human neurons or mammalian models. |
| 2023–2024 natural history | A 2024 preprint collected online data from 177 individuals and examined 57 in person. Mean Vineland Adaptive Behavior Composite was 62.9 ± 19.1; mean longitudinal change was −3.1 ± 7.3. | Longitudinal clinical and adaptive-function assessment with genotype-severity modeling documented frequent hypotonia, spasticity, ataxia, seizures, optic-nerve atrophy, cerebellar atrophy and cognitive impairment. (sudnawa2024heterogeneityofcomprehensive pages 1-5) | The cited report was a non-peer-reviewed medRxiv preprint; ascertainment and allelic heterogeneity complicate estimates. |
| 2023–2024 translational status | Translation remains early and allele-specific. An N-of-1 program screened 468 gapmers across 77 heterozygous sites and began intrathecal allele-selective ASO dose escalation at 20 mg. Fisetin restored human KIF1A-R11Q activity in vitro and improved phenotypes in model worms. | The ASO was designed to recruit RNase H1 and reduce the mutant transcript selectively. Fisetin restored ATPase activity and processive motility without affecting wild-type KIF1A in the reported assays. (ziegler2024antisenseoligonucleotidetherapy pages 5-6, chai2024aplantflavonol pages 1-2) | The ASO evidence concerns one individual. Fisetin remains preclinical and variant-specific; neither study establishes a broadly approved disease-modifying KAND therapy. |
Table: Concise evidence-based annotation of human KIF1A/Q12756, covering motor chemistry, domains, cargo transport, localization, disease mechanisms and 2023–2024 translation. Direct human or mammalian findings are distinguished from inferences based on the C. elegans ortholog UNC-104.
KIF1A belongs to the kinesin-3 subfamily and to the broader TRAFAC myosin–kinesin ATPase class. The N-terminal motor domain contains the conserved nucleotide- and microtubule-binding machinery. It is followed by a neck-coil/coiled-coil-rich stalk, an FHA domain, and a C-terminal cargo-binding region containing a pleckstrin-homology (PH) domain. The PH domain binds phosphatidylinositol-4,5-bisphosphate-containing artificial vesicles, supporting a role in motor association with lipid cargo membranes. The FHA and adjacent coiled-coil regions also participate in intramolecular regulation rather than serving merely as passive spacers. (chiba2023insightintothe pages 1-2, chai2024aplantflavonol pages 1-2)
The domain arrangement agrees with the supplied annotations Kinesin-like, KIF1-type kinesin, FHA/FHA_KIF1A, and kinesin-associated domains. No literature retrieved indicated a conflicting identity, organism or protein family.
The core reaction is:
ATP + H₂O → ADP + inorganic phosphate, coupled to conformational changes that move KIF1A along a microtubule.
In axons, most microtubules have their plus ends facing the nerve terminal. KIF1A’s plus-end-directed movement therefore produces anterograde transport, from the soma toward distal axons and presynaptic sites. ATP-binding, hydrolysis and product release coordinate the two motor heads through their neck linkers. (chiba2023insightintothe pages 1-2, benoit2024cryoemunveilskinesin pages 1-2)
A major 2024 structural advance was the determination of 2.7–3.5 Å cryo-EM structures of dimeric, microtubule-bound human KIF1A in multiple nucleotide states. One- and two-head-bound configurations were observed. In the two-head-bound state, the leading head had a backward-pointing neck linker and open nucleotide pocket, whereas the trailing head had a docked, forward-oriented neck linker and closed pocket—structural evidence for ATPase-coupled head–head coordination. The positively charged kinesin-3-specific K-loop/loop 12 contacted the negatively charged C-terminal tails of both α- and β-tubulin. These electrostatic interactions facilitate microtubule association and rapid rebinding, helping explain runs of more than 1,000 steps under suitable in-vitro conditions. (benoit2024cryoemunveilskinesin pages 1-2)
KIF1A is unusually fast and superprocessive but relatively load-sensitive. Optical-trap work found force-dependent detachment at approximately 3 pN, followed by rapid rebinding; pathogenic V8M and Y89D substitutions impaired force generation, velocity, run length and landing rate and delayed cargo transport in cells. This combination—long unloaded runs, rapid microtubule rebinding and lower load tolerance—appears adapted for long-distance vesicular transport, potentially with multiple motors cooperating on a cargo. (anazawa2022denovomutations pages 10-11)
The pathogenic P305L variant illustrates how disease can arise without simply abolishing the K-loop’s electrostatic contacts: it changes loop-12 conformation and compromises strong microtubule binding. Thus, motor-domain variants may perturb allosteric coordination, nucleotide cycling or microtubule affinity even where the principal binding residues remain present. (benoit2024cryoemunveilskinesin pages 1-2)
Current models describe soluble, cargo-free KIF1A as compact and autoinhibited, with tail/stalk regions folding back to suppress motor activity. The inactive protein is often described as predominantly monomeric in solution; activation and microtubule engagement favor dimerization and coordinated two-headed movement. The distinction is contextual rather than absolute: engineered constructs, concentration, cargo binding and cellular environment can shift the oligomeric state. (chiba2023insightintothe pages 1-2, hummel2021specifickif1a–adaptorinteractions pages 1-2)
This regulation prevents wasteful ATP consumption and unproductive microtubule movement. Cargo-associated factors can relieve autoinhibition, while the FHA/coiled-coil region contributes to maintaining the inhibited state. Importantly, disease may result from either direction of dysregulation: most studied KAND substitutions reduce transport, but some release autoinhibition and create hyperactive motors. Both insufficient and excessive cargo delivery can disrupt synaptic organization. More than 100 KAND-associated point variants had been catalogued by the 2023 review. (chiba2023insightintothe pages 1-2)
The strongest functional annotation is transport of SVPs and synaptic-vesicle-associated carriers. SV membrane proteins are synthesized in the soma and exported toward presynaptic terminals in precursor carriers. Mammalian KIF1A loss causes SVPs to accumulate in neuronal cell bodies, sharply reduces terminal synaptic-vesicle abundance, and produces sensorimotor deficits and early postnatal death in mice. These findings establish that the motor is not merely associated with SVPs but is required for their physiologically effective delivery. (vitet2023huntingtinrecruitskif1a pages 1-2, chiba2023insightintothe pages 1-2)
The distinction between mature synaptic vesicles and precursor carriers varies across experiments; the most precise general annotation is therefore anterograde transport of presynaptic vesicle precursors and synaptic-vesicle proteins.
KIF1A is also a principal anterograde motor for dense-core vesicles (DCVs) carrying neuropeptides and other secreted factors. DCVs originate at the Golgi and travel into both axons and dendrites. KIF1A additionally transports active-zone precursor material needed to assemble neurotransmitter-release sites. (chiba2023insightintothe pages 8-8, chiba2023insightintothe pages 1-2, hummel2021specifickif1a–adaptorinteractions pages 1-2)
Cargo selectivity is combinatorial rather than being determined by one universal receptor:
KIF1A is a soluble cytoplasmic motor dynamically recruited to microtubules and cargo membranes; it is not a constitutive transmembrane or fixed organelle-resident protein. Its major functional geography is neuronal: soma and Golgi-associated cargo-export regions, axonal shafts, distal axons and presynaptic terminals. It also operates in dendrites for selected cargos, particularly DCVs. (chiba2023insightintothe pages 1-2, hummel2021specifickif1a–adaptorinteractions pages 1-2)
Axonal enrichment of transport does not arise solely from intrinsic plus-end directionality. Axonal microtubules are mostly plus-end-out, whereas dendrites contain mixed-polarity arrays; cargo identity, motor activation, microtubule-associated proteins and on-vesicle regulation therefore help determine compartmental targeting. Live-neuron studies found KIF1A-associated vesicles capable of long-range movement without an absolute axonal restriction. (hummel2021specifickif1a–adaptorinteractions pages 1-2)
KIF1A participates in the presynaptic secretory and assembly pathway:
Consequently, KIF1A influences synapse number and size, release probability, neuronal maintenance and behavior. These are downstream consequences of its proximal biochemical role in cargo transport, rather than evidence that KIF1A is itself a conventional receptor or soluble signaling enzyme.
KIF1A also intersects with lysosomal and autophagic trafficking in some contexts. However, its best-established primary function remains transport of presynaptic and regulated-secretory vesicle cargo, and lysosomal assignments should not displace that central annotation. (hummel2021specifickif1a–adaptorinteractions pages 1-2)
Pathogenic KIF1A variants cause KIF1A-associated neurological disorder (KAND), an umbrella encompassing phenotypes historically classified as SPG30 hereditary spastic paraplegia, hereditary sensory/autonomic neuropathy and dominant intellectual-developmental syndromes. Open Targets independently links human KIF1A/ENSG00000130294 to hereditary spastic paraplegia 30, hereditary sensory neuropathy 2C and autosomal-dominant intellectual disability 9. (OpenTargets Search: -KIF1A)
Mechanisms are allele-specific:
For example, R11 lies near the β1 sheet and nucleotide-binding pocket; R11Q severely weakens microtubule binding even with AMP-PNP. R254 lies in loop L11 near the α4 microtubule-binding interface; R254Q particularly weakens the ADP-state interaction, consistent with excess dissociation during cycling. These results show why “KIF1A loss of function” should not be treated as one uniform molecular defect. (anazawa2022denovomutations pages 10-11)
Benoit and colleagues reported nucleotide-state cryo-EM structures of human KIF1A–microtubule complexes at 2.7–3.5 Å, defining K-loop/tubulin-tail interactions, head–head coordination and the structural effect of P305L. This provides a mechanistic framework for classifying pathogenic variants and potentially designing allele- or mechanism-specific modulators. Published July 2024, Nature Communications: https://doi.org/10.1038/s41467-024-48720-4. (benoit2024cryoemunveilskinesin pages 1-2)
The 2023 HTT study established that changing KIF1A recruitment alters SVP supply, release probability and motor learning in an intact mammalian circuit. It strengthens the expert view that KAND therapies must normalize cargo flux rather than indiscriminately stimulate KIF1A. (vitet2023huntingtinrecruitskif1a pages 1-2)
A 2024 medRxiv natural-history analysis collected online data from 177 individuals, with 57 assessed in person. Common findings included hypotonia, spasticity, ataxia, seizures, optic-nerve atrophy, cerebellar atrophy and cognitive impairment. Mean Vineland Adaptive Behavior Composite was 62.9 ± 19.1, and mean longitudinal change was −3.1 ± 7.3. Age at initial assessment and abnormal EEG/seizures were associated with decline; variant Evolutionary Scale Model scores correlated with final VABS-ABC (p=0.003), and ESM plus EEG/seizure and neuroimaging variables explained 34% of final-score variance (p<0.001). Because this version was a preprint posted 2 March 2024, its estimates should be interpreted with appropriate caution. URL: https://doi.org/10.1101/2024.02.29.24303377. (sudnawa2024heterogeneityofcomprehensive pages 1-5)
An allele-selective, N-of-1 ASO—nL-KIF1-001—was designed to recruit RNase H1 to degrade the mutant KIF1A transcript while sparing the reference allele. Investigators screened 468 gapmer ASOs across 77 heterozygous genomic sites and selected a 20-mer 5-10-5 MOE gapmer. Under FDA IND 161670, intrathecal treatment began at 20 mg, with planned 20-mg increments to at most 80 mg. Outcomes included behavioral-arrest spells, falls, six-minute walk performance, EEG, neurological examination and cognitive measures. Published August 2024 in Nature Medicine: https://doi.org/10.1038/s41591-024-03197-y. This is a real-world implementation but remains an open-label, single-patient intervention, not evidence of general efficacy across KAND. (ziegler2024antisenseoligonucleotidetherapy pages 5-6)
A 2024 PNAS study modeled KIF1A-R11Q in C. elegans. Genetic suppressors restored vesicle localization and coordinated movement. The flavonol fisetin improved worm movement and morphology and directly restored ATPase activity and processive movement of purified human KIF1A-R11Q without measurably affecting wild-type KIF1A in the reported assays. Published 25 January 2024: https://doi.org/10.1073/pnas.2311936121. This is promising proof of principle for variant-selective motor rescue, but it is preclinical and cannot presently be interpreted as a treatment recommendation. (chai2024aplantflavonol pages 1-2)
Clinical diagnostics. KIF1A is an established disease gene in sequencing panels and exome/genome interpretation for complex hereditary spastic paraplegia, sensory neuropathy, developmental delay, cerebellar atrophy, optic atrophy and epilepsy. Functional interpretation should consider variant position and mechanism rather than relying on gene-level association alone. (OpenTargets Search: -KIF1A, anazawa2022denovomutations pages 10-11)
Disease modeling. CRISPR-engineered C. elegans, purified human motor assays, optical trapping, mammalian neurons, iPSC-derived neurons and mouse circuit models are used to connect genotype to ATPase behavior, transport and neurological phenotype. Human KIF1A can rescue UNC-104-related defects in worms, supporting evolutionary conservation, but model-organism rescue does not eliminate human-specific neuronal context. (anazawa2022denovomutations pages 10-11, chai2024aplantflavonol pages 1-2)
Therapeutic development. Current strategies include allele-selective transcript reduction for dominant toxic alleles, small molecules or suppressor changes that restore weak motors, and—in principle—approaches that normalize autoinhibition or cargo engagement. Because both hypoactive and hyperactive variants cause disease, a universal KIF1A activator or inhibitor is unlikely to suit all patients. No broadly approved disease-modifying KAND therapy was identified in the retrieved evidence. (chiba2023insightintothe pages 1-2, ziegler2024antisenseoligonucleotidetherapy pages 5-6, chai2024aplantflavonol pages 1-2)
The most defensible functional annotation for human KIF1A/Q12756 is: a neuronal kinesin-3 ATPase that converts ATP hydrolysis into highly processive, microtubule-plus-end-directed transport of presynaptic and regulated-secretory vesicle precursors, with cargo-dependent activation and localization to axonal and selected dendritic transport routes. Its primary physiological role is to deliver synaptic-vesicle proteins, dense-core vesicles and active-zone material from the soma to distant neuronal compartments.
The field’s current mechanistic consensus is supported by convergent human structural biochemistry, single-molecule measurements, mammalian neuronal and mouse experiments, and conserved UNC-104 genetics. The principal uncertainty is not the core function but how individual cargos activate KIF1A in particular neuronal compartments and how each pathogenic allele shifts force, stepping, autoinhibition and cargo flux. The 2023–2024 literature strongly supports mechanism- and allele-specific therapy, while current human therapeutic evidence remains preliminary.
References
(chiba2023insightintothe pages 1-2): Kyoko Chiba, Tomoki Kita, Yuzu Anazawa, and Shinsuke Niwa. Insight into the regulation of axonal transport from the study of kif1a-associated neurological disorder. Journal of cell science, Jan 2023. URL: https://doi.org/10.1242/jcs.260742, doi:10.1242/jcs.260742. This article has 47 citations and is from a domain leading peer-reviewed journal.
(chai2024aplantflavonol pages 1-2): Yongping Chai, Dong Li, Weibin Gong, Jingyi Ke, Dianzhe Tian, Zhe Chen, Angel Guo, Zhengyang Guo, Wei Li, Wei Feng, and Guangshuo Ou. A plant flavonol and genetic suppressors rescue a pathogenic mutation associated with kinesin in neurons. Proceedings of the National Academy of Sciences of the United States of America, Jan 2024. URL: https://doi.org/10.1073/pnas.2311936121, doi:10.1073/pnas.2311936121. This article has 11 citations and is from a highest quality peer-reviewed journal.
(vitet2023huntingtinrecruitskif1a pages 1-2): Hélène Vitet, Julie Bruyère, Hao Xu, Claire Séris, Jacques Brocard, Yah-Sé Abada, Benoît Delatour, Chiara Scaramuzzino, Laurent Venance, and Frédéric Saudou. Huntingtin recruits kif1a to transport synaptic vesicle precursors along the mouse axon to support synaptic transmission and motor skill learning. eLife, Jul 2023. URL: https://doi.org/10.7554/elife.81011, doi:10.7554/elife.81011. This article has 17 citations and is from a domain leading peer-reviewed journal.
(anazawa2022denovomutations pages 10-11): Yuzu Anazawa, Tomoki Kita, Rei Iguchi, Kumiko Hayashi, and Shinsuke Niwa. De novo mutations in kif1a-associated neuronal disorder (kand) dominant-negatively inhibit motor activity and axonal transport of synaptic vesicle precursors. Aug 2022. URL: https://doi.org/10.1073/pnas.2113795119, doi:10.1073/pnas.2113795119. This article has 61 citations and is from a highest quality peer-reviewed journal.
(benoit2024cryoemunveilskinesin pages 1-2): Matthieu P.M.H. Benoit, Lu Rao, Ana B. Asenjo, Arne Gennerich, and Hernando Sosa. Cryo-em unveils kinesin kif1a’s processivity mechanism and the impact of its pathogenic variant p305l. Nature Communications, Jul 2024. URL: https://doi.org/10.1038/s41467-024-48720-4, doi:10.1038/s41467-024-48720-4. This article has 34 citations and is from a highest quality peer-reviewed journal.
(hummel2021specifickif1a–adaptorinteractions pages 1-2): Jessica J.A. Hummel and Casper C. Hoogenraad. Specific kif1a–adaptor interactions control selective cargo recognition. The Journal of Cell Biology, Jul 2021. URL: https://doi.org/10.1083/jcb.202105011, doi:10.1083/jcb.202105011. This article has 64 citations.
(chiba2023insightintothe pages 8-8): Kyoko Chiba, Tomoki Kita, Yuzu Anazawa, and Shinsuke Niwa. Insight into the regulation of axonal transport from the study of kif1a-associated neurological disorder. Journal of cell science, Jan 2023. URL: https://doi.org/10.1242/jcs.260742, doi:10.1242/jcs.260742. This article has 47 citations and is from a domain leading peer-reviewed journal.
(sudnawa2024heterogeneityofcomprehensive pages 1-5): Khemika K. Sudnawa, Wenxing Li, Sean Calamia, Cara H. Kanner, Jennifer M. Bain, Aliaa H. Abdelhakim, Alexa Geltzeiler, Caroline M. Mebane, Frank A. Provenzano, Tristan T. Sands, Robert J. Fee, Jacqueline Montes, Yufeng Shen, and Wendy K. Chung. Heterogeneity of comprehensive clinical phenotype and longitudinal adaptive function and correlation with computational predictions of severity of missense genotypes in kif1a-associated neurological disorder. MedRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.02.29.24303377, doi:10.1101/2024.02.29.24303377. This article has 18 citations.
(ziegler2024antisenseoligonucleotidetherapy pages 5-6): Alban Ziegler, Joanne Carroll, Jennifer M. Bain, Tristan T. Sands, Robert J. Fee, David Uher, Cara H. Kanner, Jacqueline Montes, Sarah Glass, Julie Douville, Laurence Mignon, Joseph G. Gleeson, Stanley T. Crooke, and Wendy K. Chung. Antisense oligonucleotide therapy in an individual with kif1a-associated neurological disorder. Nature medicine, 30:2782-2786, Aug 2024. URL: https://doi.org/10.1038/s41591-024-03197-y, doi:10.1038/s41591-024-03197-y. This article has 70 citations and is from a highest quality peer-reviewed journal.
(vitet2023huntingtinrecruitskif1a pages 25-26): Hélène Vitet, Julie Bruyère, Hao Xu, Claire Séris, Jacques Brocard, Yah-Sé Abada, Benoît Delatour, Chiara Scaramuzzino, Laurent Venance, and Frédéric Saudou. Huntingtin recruits kif1a to transport synaptic vesicle precursors along the mouse axon to support synaptic transmission and motor skill learning. eLife, Jul 2023. URL: https://doi.org/10.7554/elife.81011, doi:10.7554/elife.81011. This article has 17 citations and is from a domain leading peer-reviewed journal.
(chiba2023insightintothe pages 9-9): Kyoko Chiba, Tomoki Kita, Yuzu Anazawa, and Shinsuke Niwa. Insight into the regulation of axonal transport from the study of kif1a-associated neurological disorder. Journal of cell science, Jan 2023. URL: https://doi.org/10.1242/jcs.260742, doi:10.1242/jcs.260742. This article has 47 citations and is from a domain leading peer-reviewed journal.
(OpenTargets Search: -KIF1A): Open Targets Query (-KIF1A, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.